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2006 Fiscal Year Final Research Report Summary

Explanation of partner proteins forming complex with PHGPx of rat testis

Research Project

Project/Area Number 17570158
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Cell biology
Research InstitutionUniversity of Yamanashi

Principal Investigator

YOKOTA Sadaki  University of Yamanashi, Interdisciplinary Graduate School of Medicine and Engineering, Prof., 大学院医学工学総合研究部, 教授 (40020755)

Project Period (FY) 2005 – 2006
KeywordsPHGPx / Rat testis / complex / mitochondria / Blue native PAGE
Research Abstract

Phospholipid hydroperoxide glutathione peroxidase (PHGPx) is a selenium-containing enzyme whose major function is reduction of esterified phospholipid or peroxidized cholesterol of membrane. The enzyme is expressed in various tissues among which testis shows the highest expression. Previously we have clarified that PHGPx localizes to various subcellular compartments of rat spermatogenic cells. On the other hand, it has been proved that our peptide antibody against 15 amino acid chain at the C-terminus of human PHGPx dose not react with PHGPx in testis extract without heating and reduction of the extract. This fact suggests that PHGPx forms protein complex so that the C-terminal region is masked by binding protein. We suppose that PHGPx might have not only anti-oxidant function but also other unknown functions considering the variety of subcellular localizations and the complex formation of PHGPx. Then, we isolated active protein complexes from rat testicular mitochondrial fraction by blue native polyacrylamide electrophoresis (BN-PAGE) and analyzed the isolated complexes by SDS-PAGE and Western blotting. We found at first time that rat testicular mitochondrial PHGPx was associated with other proteins to form complexes and could be dissociated to 19 kDa PHGPx by heating and reduction, showing that binding of PHGPx with other proteins was non-covalent. The size of the complexes varied over 400 kDa to 100 kDa. This wide range of the complex size might reflect heterogeneity of the mitochondria derived from various spermatogenic cells with different developing stage. In addition, the variety of the complexes suggests different functions of the PHGPx complexes in the spermatogenic cells with each developing stage. We tried to determine partners of PHGPx by PMF analysis of subunit spots dissociated the complexes but we did not success. In next step of study, we purify each complex, analyze the subunit spots by PMF and specify the partner proteins.

  • Research Products

    (4 results)

All 2007 2005

All Journal Article (4 results)

  • [Journal Article] Possible function of caudal nuclear pocket : Degradation of nucleoproteins by ubiquitin-proteasome system in rat spermatids and human sperm.2007

    • Author(s)
      ハラグチ M.セリーナ, 他
    • Journal Title

      Journal of Histochemistry and Cytochemistry (印刷中)

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] Possible function of caudal nuclear pocket : Degradation of nucleoproteins by ubiquitin-proteasome system in rat spermatids and human sperm2007

    • Author(s)
      Celina M.Haraguchi et al.
    • Journal Title

      Journal of Histochemistry and Cytochemistry (in press)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Journal Article] Chromatoid bodies : Aggresome-like characteristics and degradation site for organelles of spermiogenic cells.2005

    • Author(s)
      ハラグチ M.セリーナ, 他
    • Journal Title

      Journal of Histochemistry and Cytochemistry 53・4

      Pages: 455-465

    • Description
      「研究成果報告書概要(和文)」より
  • [Journal Article] Chromatoid bodies : Aggresome-like characteristics and degradation sites for organelles of spermiogenic cells2005

    • Author(s)
      Celina M.Haraguchi et al.
    • Journal Title

      Journal of Histo-chemistry and Cytochemistry 53(4)

      Pages: 455-465

    • Description
      「研究成果報告書概要(欧文)」より

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Published: 2008-05-27  

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